title: The sodium effect of Bacillus subtilis growth on aspartate.
abstract: aspH mutants of Bacillus subtilis have a constitutive aspartase activity and grow well on aspartate as sole carbon source. aspH aspT mutants, which are deficient in high affinity aspartate transport as a result of the aspT mutation, grow as well as aspH mutants in medium containing high concentrations of aspartate and Na+. This Na+ effect is not due to an enhancement of aspartate transport but is the result of increased cellular metabolism. The ability to grow rapidly in sodium aspartate is induced by prior growth in the presence of Na+. In potassium aspartate, the addition of arginine, citrulline, ornithine, delta 1-pyrroline-5-carboxylase or proline instead of Na+ also allows rapid growth; but in a mutant deficient in ornithine--oxo-acid aminotransferase, only pyrroline-carboxylate or proline can replace Na+. The amino acid pool of cells growing slowly in potassium aspartate contains proline at a low concentration which increases upon addition of proline (but not Na+) to the medium. Thus, Na+ addition does not increase the synthesis of proline, but proline or pyrroline-carboxylate acts similarly to Na+ either in preventing some inhibitory effect (by aspartate or the accumulating NH4+) or in overcoming some deficiency (e.g. in further proline metabolism.
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D001224:Aspartic Acid / Q000378:metabolism*; D001412:Bacillus subtilis / Q000187:drug effects* / Q000254:growth & development / Q000378:metabolism; D009953:Ornithine-Oxo-Acid Transaminase / Q000378:metabolism; D012964:Sodium / Q000494:pharmacology*
chemical_list: D000596:Amino Acids; D001224:Aspartic Acid; D012964:Sodium; D009953:Ornithine-Oxo-Acid Transaminase